PubMed · 12038409
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Washington. 1977. Laetrile.. https://pubmed.ncbi.nlm.nih.gov/12038409/
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Amygdalin, the phytochemical responsible for the characteristic bitterness of apricot (Prunus armeniaca L.) kernels, also exhibits significant bioactive properties and therapeutic potential. Genetic regulation of amygdalin content is therefore a key objective in apricot breeding programs aimed at quality improvement. In this study, we conducted quantitative trait loci (QTL) mapping to uncover the genetic basis of sweet-bitter differentiation in apricot kernels. We identified a 15-bp insertion/deletion (indel) polymorphism strongly related to kernel bitterness, with marker validation achieving 100% concordance across 601 apricot germplasm accessions. Notably, this polymorphic site is located within the helix-loop-helix (HLH) domain of the basic HLH (bHLH) transcription factor PabHLH2. Protein interaction analyses revealed that the 15-bp deletion variant impaired dimerization capacity, reducing transcriptional activation of downstream targets. Using yeast one-hybrid screening and dual-luciferase reporter assays, we identified PaCYP71AN24 and PaCYP79D16 as direct transcriptional targets of PabHLH2. Functional characterization further indicated that the PabHLH2a variant (harboring the 15-bp insertion) significantly enhanced the promoter activity of these cytochrome P450 genes compared with the deletion variant. Transient overexpression and silencing experiments in apricot kernels further confirmed that the 15-bp insertion positively regulates both PaCYP71AN24/PaCYP79D16 expression and prunasin accumulation, the immediate biosynthetic precursor of amygdalin. Overall, these findings provide mechanistic insights into the allelic variation underlying kernel bitterness and delineate the molecular cascade of amygdalin biosynthesis. The identified molecular markers and functional characterization establish a basis for marker-assisted breeding of low-amygdalin apricot cultivars, supporting the dual-purpose utilization of kernels in food and pharmaceutical industries.
BACKGROUND: Many cancer patients treated with conventional therapies also try 'alternative' cancer treatments. Laetrile is one such 'alternative' that is claimed to be effective by many alternative therapists. Laetrile is also sometimes referred to as amygdalin, although the two are not the same. OBJECTIVE: The aim of this review is to summarize all types of clinical data related to the effectiveness or safety of laetrile interventions as a treatment of any type of cancer. MATERIALS AND METHODS: All types of clinical studies containing original clinical data of laetrile interventions were included. We searched the Cochrane Central Register of Controlled Trials (CENTRAL), MEDLINE (from 1951), EMBASE (from 1980), Allied and Complementary Medicine (AMED), Scirus, CancerLit, Cumulative Index to Nursing and Allied Health (CINAHL; all from 1982), CAMbase (from 1998), the MetaRegister, the National Research Register, and our own files. For reports on the safety of laetrile, we also searched the Uppsala database. No language restrictions were imposed. RESULTS: Thirty six reports met our inclusion criteria. No controlled clinical trials were found. Three articles were nonconsecutive case series, 2 were consecutive case series, 6 were best case series, and 25 were case reports. None of these publications proved the effectiveness of laetrile. CONCLUSION: Therefore, the claim that laetrile has beneficial effects for cancer patients is not supported by sound clinical data.
We report a novel approach for the controlled delivery of an antiinflammatory, chemopreventive drug by an enzyme-triggered drug release mechanism via the degradation of encapsulated hydrogels. The hydro- and organogelators are synthesized in high yields from renewable resources by using regioselective enzyme catalysis, and a known chemopreventive and antiinflammatory drug, i.e., curcumin, is used for the model study. The release of the drug occurred at physiological temperature, and control of the drug release rate is achieved by manipulating the enzyme concentration and/or temperature. The byproducts formed after the gel degradation were characterized and clearly demonstrated the site specificity of degradation of the gelator by enzyme catalysis. The present approach could have applications in developing cost-effective controlled drug delivery vehicles from renewable resources, with a potential impact on pharmaceutical research and molecular design and delivery strategies.